BMRB Entry 16468
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16468
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Saez, Natalie; Mobli, Mehdi; Rash, Lachlan; King, Glenn. "High-resolution solution structure of the ASIC1a blocker PcTx1" To be Published ., .-..
Assembly members:
PcTx1, polymer, 41 residues, 4792.611 Da.
Natural source: Common Name: Trinidad chevron tarantula Taxonomy ID: 179874 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Psalmopoeus cambridgei
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pLICC
Entity Sequences (FASTA):
PcTx1: SEDCIPKWKGCVNRHGDCCE
GLECWKRRRSFEVCVPKTPK
T
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 161 |
| 15N chemical shifts | 42 |
| 1H chemical shifts | 273 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PcTx1 | 1 |
Entities:
Entity 1, PcTx1 41 residues - 4792.611 Da.
Residue 1 is a vestige of the TEV cleavage site used for recombinant production of the protein.
| 1 | SER | GLU | ASP | CYS | ILE | PRO | LYS | TRP | LYS | GLY | ||||
| 2 | CYS | VAL | ASN | ARG | HIS | GLY | ASP | CYS | CYS | GLU | ||||
| 3 | GLY | LEU | GLU | CYS | TRP | LYS | ARG | ARG | ARG | SER | ||||
| 4 | PHE | GLU | VAL | CYS | VAL | PRO | LYS | THR | PRO | LYS | ||||
| 5 | THR |
Samples:
sample_1: PcTx1, [U-99% 13C; U-99% 15N], 0.3 mM; sodium phosphate buffer, pH 6.0 10 mM; D2O 7%; H2O 93%
sample_2: PcTx1, [U-99% 13C; U-99% 15N], 0.3 mM; sodium phosphate buffer, pH 6.0 10 mM; D2O 100%
sample_conditions_1: ionic strength: 10 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 4D HC(CO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement, structure solution
XEASY, Bartels et al. - chemical shift assignment
Rowland NMR Toolkit, Hoch, Stern et al. - processing
NMR spectrometers:
- Bruker Avance 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks